ID G3JBJ9_CORMM Unreviewed; 577 AA.
AC G3JBJ9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Vacuolar carboxypeptidase Cps1, putative {ECO:0000313|EMBL:EGX95304.1};
GN ORFNames=CCM_03576 {ECO:0000313|EMBL:EGX95304.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX95304.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX95304.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX95304.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; JH126400; EGX95304.1; -; Genomic_DNA.
DR RefSeq; XP_006668790.1; XM_006668727.1.
DR AlphaFoldDB; G3JBJ9; -.
DR STRING; 983644.G3JBJ9; -.
DR GeneID; 18165602; -.
DR KEGG; cmt:CCM_03576; -.
DR VEuPathDB; FungiDB:CCM_03576; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_11_0_1; -.
DR InParanoid; G3JBJ9; -.
DR OMA; KGHVDIW; -.
DR OrthoDB; 3672990at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05674; M20_yscS; 1.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR017141; Pept_M20_carboxypep.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EGX95304.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037217-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037217-2}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..577
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003446071"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
SQ SEQUENCE 577 AA; 62016 MW; 0B6BC5BD67DAD7D3 CRC64;
MAFSKLALLA SAAACVSALA VPSPVRSIID TASDECRLPP PIDPSGDRLP HSSALWGGAA
ALRLQVRRHQ AVVRVPSICY DDLGAIGHDG RWAPFDQLHR VLRKTYPTLN EDPSKANAGS
RYKHAAVETI NTYGLLYTVR GSDPALKPVL LMAHQDVVPV ADASTWTHPP FAAHYDGQFL
WGRGASDDKN SLTALLSTLE TMLSLRSWKP RRTVLVSLGF DEECSGFRGA AHIAAELTSR
YGDGGLAVVL DEGGFGIQTV GDVKYVLPSI TEKGHVDVWF DLDVIGGHSS IPAPHTGIGI
VAEIVAALEA HPYAPVLTTA NPVYAHMACL ARYSPAARPE ITERVRSGDV QGLAAVLDAA
GAAEAYTVRT AQAVDFIRGG QKINAMPEKV TLGVNYRVTL DDGIYKVLHN IVKYVDPVVK
RYNLSVAAFE GDDGYAAYAA KAGAPVDAAY ATNAKGKLTI KTAETSQPAP VSPMHGKVWD
TFSGTAQHTL AFDGTVVPVG ETMTGNTDTR HYQNLTPNIY RFTPAAAGSS YNIHTIDERV
DMHEHMKMIA FYYDFVRNFD AAVLEGESAP ELDNLEL
//
